ISOTHERMAL COMPRESSIBILITY STUDIES OF DIPEPTIDE IN AQUEOUS SODIUM CHLORIDE SOLUTION

Abstract

Protein hydration plays a crucial role in stabilizing the native structure of globular proteins in aqueous solutions. The specific interactions of water with various functional groups on the proteins as well as other solvent-related effects contribute to the formation of the stable folded structure of proteins in solutions. Thus, it is of immense importance to study the low-molecular –weight model compounds such as amino acids, peptides, and their derivatives, which represent the building blocks of proteins in a variety of media. The conformational transitions of biopolymers are extremely sensitive to subtle changes in solvent medium. Therefore, in order to understand the behavior of proteins in aqueous salt solutions, we have studied the isothermal compressibility and their derived parameters of glycylglycine in aqueous electrolyte solutions.